O-Glycosylation of Nuclear and Cytosolic Proteins
نویسندگان
چکیده
1Graduate Program, Department of Biochemistry and Molecular Genetics, The University of Alabama at Birmingham, Birmingham, AL 35294 2Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205-2185 §To whom correspondence should be addressed. * The authors’ work was supported by NIH Grants HD 13563 and CA 42486 as well as grants from the Juvenile Diabetes Foundation and the American Health Assistance Foundation to GWH and a National Science Foundation predoctoral fellowship to FIC.
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Potential regulation of nuclear UDP-N-acetylglucosaminyl transferase (OGT) by substrate availability: ability of chromatin protein to bind UDP-N-acetylglucosamine and reduce OGT-mediated O-Linked glycosylation.
UDP-N-acetylglucosaminyl transferase (OGT) resides in both cytosolic and nuclear compartments and catalyzes O-linked glycosylation of various proteins. In the current study, we have extracted protein from nuclear DNA (chromatin protein) using 0.2% NP-40 detergent. Addition of chromatin protein to either cytosolic or nuclear preparations (containing abundant OGT) resulted in a dose-dependent los...
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O-linked beta-N-acetylglucosamine (O-GlcNAc) is both an abundant and dynamic posttranslational modification similar to phosphorylation that occurs on serine and threonine residues of cytosolic and nuclear proteins in all metazoans and cell types examined, including cardiovascular tissue. Since the discovery of O-GlcNAc more than 20 years ago, the elucidation of O-GlcNAc as a posttranslational m...
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